ArticleThe EMBO journal2010
Calmodulin dissociation regulates Myo5 recruitment and function at endocytic sites.
Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Food nanoparticles from rice vinegar: isolation, characterization, and antioxidant activities.NPJ science of food · 2022Article
- Coupled sterol synthesis and transport machineries at ER-endocytic contact sites.The Journal of cell biology · 2021Article
- Human myosin 1e tail but not motor domain replaces fission yeast Myo1 domains to support myosin-I function during endocytosis.Experimental cell research · 2019Article
- TheJournal of cell science · 2019Article
- Article
- Yeast-model-based study identified myosin- and calcium-dependent calmodulin signalling as a potential target for drug intervention in chorea-acanthocytosis.Disease models & mechanisms · 2019Article
- Article
- Calmodulin Promotes N-BAR Domain-Mediated Membrane Constriction and Endocytosis.Developmental cell · 2016Article
- An Engineered Minimal WASP-Myosin Fusion Protein Reveals Essential Functions for Endocytosis.Developmental cell · 2015Article
- Evolution of the SH3 Domain Specificity Landscape in Yeasts.PloS one · 2015Article
- Zooming in on the molecular mechanisms of endocytic budding by time-resolved electron microscopy.Cellular and molecular life sciences : CMLS · 2014Review
- Role of Scd5, a protein phosphatase-1 targeting protein, in phosphoregulation of Sla1 during endocytosis.Journal of cell science · 2012Article
- Ultrastructural dynamics of proteins involved in endocytic budding.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Lessons from yeast for clathrin-mediated endocytosis.Nature cell biology · 2011Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
Myosins-I are conserved proteins that bear an N-terminal motor head followed by a Tail Homology 1 (TH1) lipid-binding domain. Some myosins-I have an additional C-terminal extension (C(ext)) that promotes Arp2/3 complex-dependent actin polymerization. The head and the tail are separated by a neck that binds calmodulin or calmodulin-related light chains. Myosins-I are known to participate in actin-dependent membrane remodelling. However, the molecular mechanisms controlling their recruitment and their biochemical activities in vivo are far from being understood. In this study, we provided evidence suggesting the existence of an inhibitory interaction between the TH1 domain of the yeast myosin-I Myo5 and its C(ext). The TH1 domain prevented binding of the Myo5 C(ext) to the yeast WIP homologue Vrp1, Myo5 C(ext)-induced actin polymerization and recruitment of the Myo5 C(ext) to endocytic sites. Our data also indicated that calmodulin dissociation from Myo5 weakened the interaction between the neck and TH1 domains and the C(ext). Concomitantly, calmodulin dissociation triggered Myo5 binding to Vrp1, extended the myosin-I lifespan at endocytic sites and activated Myo5-induced actin polymerization.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.